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Related Concept Videos

Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

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Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with...
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Rab Proteins01:14

Rab Proteins

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Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
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Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

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Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
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Membrane Fluidity01:26

Membrane Fluidity

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Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is...
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Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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Fluid Mosaic Model01:19

Fluid Mosaic Model

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Scientists identified the plasma membrane in the 1890s and its principal chemical components (lipids and proteins) by 1915. The model for plasma membrane structure, proposed in 1935 by Hugh Davson and James Danielli, was the first model to be widely accepted in the scientific community. The model was based on the plasma membrane's "railroad track" appearance in early electron micrographs. Davson and Danielli theorized that the plasma membrane's structure resembled a sandwich...
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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

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RAS-membrane interaction and oligomerization: there is more than meets the eye.

Abraham C Sianoya1,2, Vijay K Bhardwaj1, Alemayehu A Gorfe1,3

  • 1Department of Integrative Biology and Pharmacology, McGovern Medical School, The University of Texas Health Science Center at Houston, Houston, Texas 77030, U.S.A.

Biochemical Society Transactions
|August 13, 2025
PubMed
Summary

Rat sarcoma (RAS) proteins bind to cell membranes, which is crucial for their signaling and cancer-causing roles. This review explores how RAS proteins interact with membranes, form dimers, and potentially create larger groups, offering insights for cancer therapy.

Keywords:
RAS proteinconformational dynamicsmembrane lipidsplasma membranesignal transduction

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Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study
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Area of Science:

  • Molecular biology
  • Cellular signaling
  • Oncology

Background:

  • Membrane association is critical for Rat sarcoma (RAS) protein function in both normal signaling and oncogenic transformation.
  • Understanding RAS-membrane interactions is key to deciphering its role in cancer development.

Purpose of the Study:

  • To review recent advancements in the study of RAS-membrane interactions.
  • To emphasize the molecular mechanisms of RAS membrane engagement and oligomerization.
  • To propose new therapeutic strategies for RAS-driven cancers.

Main Methods:

  • Literature review of recent studies on RAS-membrane interactions.
  • Analysis of molecular mechanisms involving RAS lipid modification and C-terminal conformational diversity.
  • Examination of evidence for RAS dimerization and higher-order oligomerization.

Main Results:

  • RAS lipid modification and C-terminal conformational flexibility are key to membrane association.
  • The formation of RAS dimers and higher-order oligomers is under investigation, with potential implications for signaling.
  • Emerging insights suggest specific driving forces for RAS oligomerization.

Conclusions:

  • RAS membrane engagement and oligomerization are complex processes fundamental to its oncogenic function.
  • Further research into RAS oligomerization mechanisms may reveal novel therapeutic targets for RAS-driven cancers.